World Library  
Flag as Inappropriate
Email this Article

CD82 (gene)

Article Id: WHEBN0014723892
Reproduction Date:

Title: CD82 (gene)  
Author: World Heritage Encyclopedia
Language: English
Subject: CD63, CD37, CD53, CD151, CD9
Collection: Clusters of Differentiation
Publisher: World Heritage Encyclopedia

CD82 (gene)

CD82 molecule
Symbols  ; 4F9; C33; GR15; IA4; KAI1; R2; SAR2; ST6; TSPAN27
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

CD82 (Cluster of Differentiation 82) is a human protein encoded by the CD82 gene.[1] This metastasis suppressor gene product is a membrane glycoprotein that is a member of the transmembrane 4 superfamily. Expression of this gene has been shown to be downregulated in tumor progression of human cancers and can be activated by p53 through a consensus binding sequence in the promoter. Its expression and that of p53 are strongly correlated, and the loss of expression of these two proteins is associated with poor survival for prostate cancer patients. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[1]


  • Interactions 1
  • See also 2
  • References 3
  • Further reading 4
  • External links 5


CD82 (gene) has been shown to interact with CD19,[2][3] CD63[4] and CD234

See also


  1. ^ a b "Entrez Gene: CD82 CD82 molecule". 
  2. ^ Imai, T; Kakizaki M; Nishimura M; Yoshie O (August 1995). "Molecular analyses of the association of CD4 with two members of the transmembrane 4 superfamily, CD81 and CD82". J. Immunol. (UNITED STATES) 155 (3): 1229–39.  
  3. ^ Horváth, G; Serru V; Clay D; Billard M; Boucheix C; Rubinstein E (November 1998). "CD19 is linked to the integrin-associated tetraspans CD9, CD81, and CD82". J. Biol. Chem. (UNITED STATES) 273 (46): 30537–43.  
  4. ^ Hammond, C; Denzin L K; Pan M; Griffith J M; Geuze H J; Cresswell P (October 1998). "The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules". J. Immunol. (UNITED STATES) 161 (7): 3282–91.  

Further reading

  • Baek SH (2006). "A novel link between SUMO modification and cancer metastasis.". Cell Cycle 5 (14): 1492–5.  
  • Imai T, Fukudome K, Takagi S, et al. (1992). "C33 antigen recognized by monoclonal antibodies inhibitory to human T cell leukemia virus type 1-induced syncytium formation is a member of a new family of transmembrane proteins including CD9, CD37, CD53, and CD63.". J. Immunol. 149 (9): 2879–86.  
  • Ichikawa T, Ichikawa Y, Dong J, et al. (1992). "Localization of metastasis suppressor gene(s) for prostatic cancer to the short arm of human chromosome 11.". Cancer Res. 52 (12): 3486–90.  
  • Gaugitsch HW, Hofer E, Huber NE, et al. (1991). "A new superfamily of lymphoid and melanoma cell proteins with extensive homology to Schistosoma mansoni antigen Sm23.". Eur. J. Immunol. 21 (2): 377–83.  
  • Ichikawa T, Ichikawa Y, Isaacs JT (1991). "Genetic factors and suppression of metastatic ability of prostatic cancer.". Cancer Res. 51 (14): 3788–92.  
  • Imai T, Kakizaki M, Nishimura M, Yoshie O (1995). "Molecular analyses of the association of CD4 with two members of the transmembrane 4 superfamily, CD81 and CD82.". J. Immunol. 155 (3): 1229–39.  
  • Dong JT, Lamb PW, Rinker-Schaeffer CW, et al. (1995). "KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2.". Science 268 (5212): 884–6.  
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4.  
  • Mannion BA, Berditchevski F, Kraeft SK, et al. (1996). "Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29).". J. Immunol. 157 (5): 2039–47.  
  • Szöllósi J, Horejsí V, Bene L, et al. (1996). "Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY.". J. Immunol. 157 (7): 2939–46.  
  • Dong JT, Isaacs WB, Barrett JC, Isaacs JT (1997). "Genomic organization of the human KAI1 metastasis-suppressor gene.". Genomics 41 (1): 25–32.  
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56.  
  • Hammond C, Denzin LK, Pan M, et al. (1998). "The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules.". J. Immunol. 161 (7): 3282–91.  
  • Horváth G, Serru V, Clay D, et al. (1998). "CD19 is linked to the integrin-associated tetraspans CD9, CD81, and CD82.". J. Biol. Chem. 273 (46): 30537–43.  
  • Serru V, Le Naour F, Billard M, et al. (1999). "Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions.". Biochem. J. 340 (1): 103–11.  
  • Lombardi DP, Geradts J, Foley JF, et al. (1999). "Loss of KAI1 expression in the progression of colorectal cancer.". Cancer Res. 59 (22): 5724–31.  
  • Shibagaki N, Hanada K, Yamashita H, et al. (2000). "Overexpression of CD82 on human T cells enhances LFA-1 / ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation.". Eur. J. Immunol. 29 (12): 4081–91.  
  • Nakamura K, Mitamura T, Takahashi T, et al. (2000). "Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity.". J. Biol. Chem. 275 (24): 18284–90.  
  • Odintsova E, Sugiura T, Berditchevski F (2001). "Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1.". Curr. Biol. 10 (16): 1009–12.  
  • Ono M, Handa K, Withers DA, Hakomori S (2001). "Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional alpha3, alpha5-CD82 glycosylation complex in ldlD 14 cells.". Biochem. Biophys. Res. Commun. 279 (3): 744–50.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.